CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007387
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ER-retained PMA1-suppressing protein 1 
Protein Synonyms/Alias
  
Gene Name
 EPS1 
Gene Synonyms/Alias
 YIL005W; YIA5W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
586GDVIIIDKSNNYYYNubiquitination[1]
594SNNYYYNKDNFGNSLubiquitination[1]
696GILGNMEKKKNQD**ubiquitination[2]
Reference
 [1] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301] 
Functional Description
 Acts as a membrane-bound chaperone in endoplasmic reticulum quality control. Probably facilitates presentation of substrate to membrane-bound components of the degradation machinery. 
Sequence Annotation
 DOMAIN 28 142 Thioredoxin 1.
 DOMAIN 408 446 Thioredoxin 2.
 CARBOHYD 85 85 N-linked (GlcNAc...) (Potential).
 CARBOHYD 264 264 N-linked (GlcNAc...) (Potential).
 CARBOHYD 299 299 N-linked (GlcNAc...) (Potential).
 CARBOHYD 370 370 N-linked (GlcNAc...) (Potential).
 DISULFID 60 63 Redox-active (By similarity).
 DISULFID 200 203 Redox-active (By similarity).  
Keyword
 Chaperone; Complete proteome; Disulfide bond; Endoplasmic reticulum; Glycoprotein; Isomerase; Membrane; Redox-active center; Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 701 AA 
Protein Sequence
MKMNLKRLVV TFFSCITFLL KFTIAAAEPP EGFPEPLNPT NFKEELSKGL HIIDFYSPYC 60
PHCKHLAPVW METWEEFKEE SKTLNITFSQ VNCIESADLC GDENIEYFPE IRLYNPSGYI 120
KSFTETPRTK ESLIAFARRE SMDPNNLDTD LDSAKSESQY LEGFDFLELI AGKATRPHLV 180
SFWPTKDMKN SDDSLEFKNC DKCHEFQRTW KIISRQLAVD DINTGHVNCE SNPTICEELG 240
FGDLVKITNH RADREPKVAL VLPNKTSNNL FDYPNGYSAK SDGYVDFARR TFTNSKFPNI 300
TEGELEKKAN RDIDFLQERG RVTNNDIHLV FSYDPETVVI EDFDILEYLI EPLSKIPNIY 360
LHQIDKNLIN LSRNLFGRMY EKINYDASQT QKVFNKEYFT MNTVTQLPTF FMFKDGDPIS 420
YVFPGYSTTE MRNIDAIMDW VKKYSNPLVT EVDSSNLKKL ISFQTKSYSD LAIQLISSTD 480
HKHIKGSNKL IKNLLLASWE YEHIRMENNF EEINERRARK ADGIKKIKEK KAPANKIVDK 540
MREEIPHMDQ KKLLLGYLDI SKEKNFFRKY GITGEYKIGD VIIIDKSNNY YYNKDNFGNS 600
LTSNNPQLLR EAFVSLNIPS KALYSSKLKG RLINSPFHNV LSFLDIIHGN GMPGYLIVIV 660
LFIAILKGPS IYRRYKVRKH YRAKRNAVGI LGNMEKKKNQ D 701 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IDA:SGD.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0051087; F:chaperone binding; IDA:SGD.
 GO:0003756; F:protein disulfide isomerase activity; IMP:SGD.
 GO:0051082; F:unfolded protein binding; IDA:SGD.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0030433; P:ER-associated protein catabolic process; IMP:SGD.
 GO:0006621; P:protein retention in ER lumen; IMP:SGD. 
Interpro
 IPR012336; Thioredoxin-like_fold.
 IPR017937; Thioredoxin_CS.
 IPR013766; Thioredoxin_domain. 
Pfam
 PF00085; Thioredoxin 
SMART
  
PROSITE
 PS00194; THIOREDOXIN_1
 PS51352; THIOREDOXIN_2 
PRINTS